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First published online September 15, 2004
Journal of Experimental Biology 207, 3649-3656 (2004)
Published by The Company of Biologists 2004
doi: 10.1242/jeb.01219
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Regulation of heat shock genes in isolated hepatocytes from an Antarctic fish, Trematomus bernacchii

Bradley A. Buckley*, Sean P. Place and Gretchen E. Hofmann{dagger}

Department of Ecology, Evolution and Marine Biology, University of California, Santa Barbara, CA 93106-9610, USA

{dagger} Author for correspondence (e-mail: hofmann{at}lifesci.ucsb.edu)

Accepted 2 August 2004

The Antarctic fishes, isolated over evolutionary history in the sub-zero waters of the Southern Ocean, are an ideal group for studying the processes of cold adaptation. One species of Antarctic notothenioid fish, Trematomus bernacchii, has lost the ability to induce heat shock proteins (Hsps) in response to exposure to acute thermal stress or to the toxic heavy metal cadmium, an important part of the cellular defense response to such stressors. To elucidate the mechanism responsible for the lack of Hsp induction, we examined several stages of the hsp gene expression pathway, including transcription factor activity, Hsp70 mRNA production and protein synthesis patterns, in hepatocytes from T. bernacchii. Hsp70 mRNA was detected, as was heat shock factor 1 (HSF1) with DNA-binding activity. However, exposure to elevated temperature and to chemical inducers of the heat shock response failed to increase Hsp70 mRNA levels, HSF1 activity or the concentration of any size class of Hsps. These results suggest that Hsps, inducible in nearly every other species, are expressed constitutively in the cold-adapted T. bernacchii.

Key words: heat shock protein, Hsp70, hepatocyte, constitutive expression, Trematomus bernacchii, Notothenioid, Antarctica


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